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P46821

- MAP1B_HUMAN

UniProt

P46821 - MAP1B_HUMAN

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Protein

Microtubule-associated protein 1B

Gene

MAP1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Facilitates tyrosination of alpha-tubulin in neuronal microtubules By similarity. Phosphorylated MAP1B may play a role in the cytoskeletal changes that accompany neurite extension. Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing.By similarity1 Publication

GO - Molecular functioni

  1. structural molecule activity Source: ProtInc

GO - Biological processi

  1. axon extension Source: Ensembl
  2. cellular process Source: DFLAT
  3. dendrite development Source: Ensembl
  4. establishment of monopolar cell polarity Source: Ensembl
  5. microtubule bundle formation Source: Ensembl
  6. mitochondrion transport along microtubule Source: Ensembl
  7. negative regulation of intracellular transport Source: Ensembl
  8. positive regulation of axon extension Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein 1B
Short name:
MAP-1B
Cleaved into the following 2 chains:
Gene namesi
Name:MAP1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:6836. MAP1B.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication. Cytoplasm 1 Publication. Cell junctionsynapse By similarity. Cell projectiondendritic spine By similarity
Note: Colocalizes with DAPK1 in the microtubules and cortical actin fibers.By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell projection Source: UniProtKB-KW
  3. cytoplasm Source: HPA
  4. cytosol Source: Ensembl
  5. microtubule Source: UniProtKB-KW
  6. microtubule associated complex Source: ProtInc
  7. plasma membrane Source: DFLAT
  8. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Microtubule, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30581.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 24682467Microtubule-associated protein 1BPRO_0000018604Add
BLAST
Chaini2 – 22062205MAP1B heavy chainPRO_0000418379Add
BLAST
Chaini2207 – 2468262MAP1 light chain LC1PRO_0000018605Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei336 – 3361Phosphoserine1 Publication
Modified residuei541 – 5411PhosphoserineBy similarity
Modified residuei544 – 5441PhosphoserineBy similarity
Modified residuei561 – 5611PhosphoserineBy similarity
Modified residuei614 – 6141PhosphoserineBy similarity
Modified residuei828 – 8281Phosphoserine1 Publication
Modified residuei831 – 8311Phosphoserine2 Publications
Modified residuei832 – 8321Phosphoserine2 Publications
Modified residuei937 – 9371Phosphoserine1 Publication
Modified residuei992 – 9921Phosphoserine2 Publications
Modified residuei995 – 9951Phosphoserine2 Publications
Modified residuei1016 – 10161Phosphoserine3 Publications
Modified residuei1144 – 11441Phosphoserine1 Publication
Modified residuei1154 – 11541Phosphoserine1 Publication
Modified residuei1156 – 11561Phosphoserine1 Publication
Modified residuei1208 – 12081Phosphoserine1 Publication
Modified residuei1252 – 12521Phosphoserine1 Publication
Modified residuei1256 – 12561Phosphoserine1 Publication
Modified residuei1260 – 12601Phosphoserine1 Publication
Modified residuei1265 – 12651Phosphoserine2 Publications
Modified residuei1276 – 12761Phosphoserine1 Publication
Modified residuei1280 – 12801Phosphoserine1 Publication
Modified residuei1282 – 12821Phosphothreonine2 Publications
Modified residuei1312 – 13121PhosphoserineBy similarity
Modified residuei1378 – 13781Phosphoserine1 Publication
Modified residuei1387 – 13871Phosphoserine1 Publication
Modified residuei1389 – 13891Phosphoserine1 Publication
Modified residuei1396 – 13961Phosphoserine2 Publications
Modified residuei1400 – 14001Phosphoserine3 Publications
Modified residuei1427 – 14271Phosphoserine3 Publications
Modified residuei1438 – 14381Phosphoserine2 Publications
Modified residuei1443 – 14431Phosphoserine2 Publications
Modified residuei1501 – 15011Phosphoserine2 Publications
Modified residuei1618 – 16181Phosphoserine1 Publication
Modified residuei1620 – 16201Phosphoserine1 Publication
Modified residuei1625 – 16251Phosphoserine1 Publication
Modified residuei1653 – 16531Phosphoserine1 Publication
Modified residuei1779 – 17791Phosphoserine3 Publications
Modified residuei1782 – 17821Phosphoserine2 Publications
Modified residuei1785 – 17851Phosphoserine1 Publication
Modified residuei1788 – 17881Phosphothreonine2 Publications
Modified residuei1797 – 17971Phosphoserine1 Publication
Modified residuei1915 – 19151Phosphoserine1 Publication
Modified residuei1917 – 19171Phosphoserine1 Publication
Modified residuei1965 – 19651Phosphoserine1 Publication
Modified residuei2271 – 22711Phosphoserine1 Publication
Modified residuei2289 – 22891Phosphoserine1 Publication
Modified residuei2464 – 24641S-nitrosocysteineBy similarity

Post-translational modificationi

LC1 is generated from MAP1B by proteolytic processing.1 Publication
S-nitrosylation at Cys-2464 enhances interaction with microtubules, and may act as an effector modification for neuronal nitric oxide synthase control of growth-cone size, growth-cone collapse and axon retraction.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiP46821.
PaxDbiP46821.
PRIDEiP46821.

PTM databases

PhosphoSiteiP46821.

Expressioni

Gene expression databases

BgeeiP46821.
CleanExiHS_MAP1B.
ExpressionAtlasiP46821. baseline and differential.
GenevestigatoriP46821.

Organism-specific databases

HPAiCAB009792.
HPA022275.

Interactioni

Subunit structurei

3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. LC1 interacts with the amino-terminal region of MAP1B. Interacts with ANP32A and TIAM2. Interacts with the tubulin tyrosine TTL By similarity. Interacts (via C-terminus) with GAN (via Kelch domains). Interacts (via N-terminus) with DAPK1. Interacts with TMEM185A. Interacts with MAP1LC3B.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GANQ9H2C03EBI-764611,EBI-764342
LRRK2Q5S0075EBI-9517186,EBI-5323863
TP53P046376EBI-764611,EBI-366083

Protein-protein interaction databases

BioGridi110304. 45 interactions.
DIPiDIP-33474N.
IntActiP46821. 28 interactions.
MINTiMINT-243072.
STRINGi9606.ENSP00000296755.

Structurei

3D structure databases

ProteinModelPortaliP46821.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1878 – 189417MAP1B 1Add
BLAST
Repeati1895 – 191117MAP1B 2Add
BLAST
Repeati1912 – 192817MAP1B 3Add
BLAST
Repeati1929 – 194517MAP1B 4Add
BLAST
Repeati1946 – 196217MAP1B 5Add
BLAST
Repeati1963 – 197917MAP1B 6Add
BLAST
Repeati1997 – 201317MAP1B 7Add
BLAST
Repeati2014 – 203017MAP1B 8Add
BLAST
Repeati2031 – 204717MAP1B 9Add
BLAST
Repeati2048 – 206417MAP1B 10Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2294 – 2468175Mediates interaction with TMEM185AAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi589 – 790202Lys-rich (highly basic, contains many KKEE and KKEI/V repeats)Add
BLAST

Domaini

Has a highly basic region with many copies of the sequence KKEE and KKEI/V, repeated but not at fixed intervals, which is responsible for the binding of MAP1B to microtubules.

Sequence similaritiesi

Belongs to the MAP1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00550000074593.
HOGENOMiHOG000063256.
HOVERGENiHBG052409.
InParanoidiP46821.
KOiK10429.
OMAiRTPVQDH.
OrthoDBiEOG773XKP.
PhylomeDBiP46821.
TreeFamiTF350229.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR001279. Beta-lactamas-like.
IPR026074. MAP1.
IPR027321. MAP1B.
IPR000102. MAP1B_neuraxin.
[Graphical view]
PANTHERiPTHR13843. PTHR13843. 1 hit.
PTHR13843:SF5. PTHR13843:SF5. 1 hit.
PfamiPF00414. MAP1B_neuraxin. 5 hits.
[Graphical view]
PROSITEiPS00230. MAP1B_NEURAXIN. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46821-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATVVVEATE PEPSGSIANP AASTSPSLSH RFLDSKFYLL VVVGEIVTEE
60 70 80 90 100
HLRRAIGNIE LGIRSWDTNL IECNLDQELK LFVSRHSARF SPEVPGQKIL
110 120 130 140 150
HHRSDVLETV VLINPSDEAV STEVRLMITD AARHKLLVLT GQCFENTGEL
160 170 180 190 200
ILQSGSFSFQ NFIEIFTDQE IGELLSTTHP ANKASLTLFC PEEGDWKNSN
210 220 230 240 250
LDRHNLQDFI NIKLNSASIL PEMEGLSEFT EYLSESVEVP SPFDILEPPT
260 270 280 290 300
SGGFLKLSKP CCYIFPGGRG DSALFAVNGF NMLINGGSER KSCFWKLIRH
310 320 330 340 350
LDRVDSILLT HIGDDNLPGI NSMLQRKIAE LEEEQSQGST TNSDWMKNLI
360 370 380 390 400
SPDLGVVFLN VPENLKNPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR
410 420 430 440 450
SVGNTIDPVI LFQKMGVGKL EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE
460 470 480 490 500
FILPNGQEVD LPISYLTSVS SLIVWHPANP AEKIIRVLFP GNSTQYNILE
510 520 530 540 550
GLEKLKHLDF LKQPLATQKD LTGQVPTPVV KQTKLKQRAD SRESLKPAAK
560 570 580 590 600
PLPSKSVRKE SKEETPEVTK VNHVEKPPKV ESKEKVMVKK DKPIKTETKP
610 620 630 640 650
SVTEKEVPSK EEPSPVKAEV AEKQATDVKP KAAKEKTVKK ETKVKPEDKK
660 670 680 690 700
EEKEKPKKEV AKKEDKTPIK KEEKPKKEEV KKEVKKEIKK EEKKEPKKEV
710 720 730 740 750
KKETPPKEVK KEVKKEEKKE VKKEEKEPKK EIKKLPKDAK KSSTPLSEAK
760 770 780 790 800
KPAALKPKVP KKEESVKKDS VAAGKPKEKG KIKVIKKEGK AAEAVAAAVG
810 820 830 840 850
TGATTAAVMA AAGIAAIGPA KELEAERSLM SSPEDLTKDF EELKAEEVDV
860 870 880 890 900
TKDIKPQLEL IEDEEKLKET EPVEAYVIQK EREVTKGPAE SPDEGITTTE
910 920 930 940 950
GEGECEQTPE ELEPVEKQGV DDIEKFEDEG AGFEESSETG DYEEKAETEE
960 970 980 990 1000
AEEPEEDGEE HVCVSASKHS PTEDEESAKA EADAYIREKR ESVASGDDRA
1010 1020 1030 1040 1050
EEDMDEAIEK GEAEQSEEEA DEEDKAEDAR EEEYEPEKME AEDYVMAVVD
1060 1070 1080 1090 1100
KAAEAGGAEE QYGFLTTPTK QLGAQSPGRE PASSIHDETL PGGSESEATA
1110 1120 1130 1140 1150
SDEENREDQP EEFTATSGYT QSTIEISSEP TPMDEMSTPR DVMSDETNNE
1160 1170 1180 1190 1200
ETESPSQEFV NITKYESSLY SQEYSKPADV TPLNGFSEGS KTDATDGKDY
1210 1220 1230 1240 1250
NASASTISPP SSMEEDKFSR SALRDAYCSE VKASTTLDIK DSISAVSSEK
1260 1270 1280 1290 1300
VSPSKSPSLS PSPPSPLEKT PLGERSVNFS LTPNEIKVSA EAEVAPVSPE
1310 1320 1330 1340 1350
VTQEVVEEHC ASPEDKTLEV VSPSQSVTGS AGHTPYYQSP TDEKSSHLPT
1360 1370 1380 1390 1400
EVIEKPPAVP VSFEFSDAKD ENERASVSPM DEPVPDSESP IEKVLSPLRS
1410 1420 1430 1440 1450
PPLIGSESAY ESFLSADDKA SGRGAESPFE EKSGKQGSPD QVSPVSEMTS
1460 1470 1480 1490 1500
TSLYQDKQEG KSTDFAPIKE DFGQEKKTDD VEAMSSQPAL ALDERKLGDV
1510 1520 1530 1540 1550
SPTQIDVSQF GSFKEDTKMS ISEGTVSDKS ATPVDEGVAE DTYSHMEGVA
1560 1570 1580 1590 1600
SVSTASVATS SFPEPTTDDV SPSLHAEVGS PHSTEVDDSL SVSVVQTPTT
1610 1620 1630 1640 1650
FQETEMSPSK EECPRPMSIS PPDFSPKTAK SRTPVQDHRS EQSSMSIEFG
1660 1670 1680 1690 1700
QESPEQSLAM DFSRQSPDHP TVGAGVLHIT ENGPTEVDYS PSDMQDSSLS
1710 1720 1730 1740 1750
HKIPPMEEPS YTQDNDLSEL ISVSQVEASP STSSAHTPSQ IASPLQEDTL
1760 1770 1780 1790 1800
SDVAPPRDMS LYASLTSEKV QSLEGEKLSP KSDISPLTPR ESSPLYSPTF
1810 1820 1830 1840 1850
SDSTSAVKEK TATCHSSSSP PIDAASAEPY GFRASVLFDT MQHHLALNRD
1860 1870 1880 1890 1900
LSTPGLEKDS GGKTPGDFSY AYQKPEETTR SPDEEDYDYE SYEKTTRTSD
1910 1920 1930 1940 1950
VGGYYYEKIE RTTKSPSDSG YSYETIGKTT KTPEDGDYSY EIIEKTTRTP
1960 1970 1980 1990 2000
EEGGYSYDIS EKTTSPPEVS GYSYEKTERS RRLLDDISNG YDDSEDGGHT
2010 2020 2030 2040 2050
LGDPSYSYET TEKITSFPES EGYSYETSTK TTRTPDTSTY CYETAEKITR
2060 2070 2080 2090 2100
TPQASTYSYE TSDLCYTAEK KSPSEARQDV DLCLVSSCEY KHPKTELSPS
2110 2120 2130 2140 2150
FINPNPLEWF ASEEPTEESE KPLTQSGGAP PPPGGKQQGR QCDETPPTSV
2160 2170 2180 2190 2200
SESAPSQTDS DVPPETEECP SITADANIDS EDESETIPTD KTVTYKHMDP
2210 2220 2230 2240 2250
PPAPVQDRSP SPRHPDVSMV DPEALAIEQN LGKALKKDLK EKTKTKKPGT
2260 2270 2280 2290 2300
KTKSSSPVKK SDGKSKPLAA SPKPAGLKES SDKVSRVASP KKKESVEKAA
2310 2320 2330 2340 2350
KPTTTPEVKA ARGEEKDKET KNAANASASK SAKTATAGPG TTKTTKSSAV
2360 2370 2380 2390 2400
PPGLPVYLDL CYIPNHSNSK NVDVEFFKRV RSSYYVVSGN DPAAEEPSRA
2410 2420 2430 2440 2450
VLDALLEGKA QWGSNMQVTL IPTHDSEVMR EWYQETHEKQ QDLNIMVLAS
2460
SSTVVMQDES FPACKIEL
Length:2,468
Mass (Da):270,634
Last modified:January 11, 2011 - v2
Checksum:i3FFDCB2E20049A8A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti326 – 3261R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036016
Natural varianti574 – 5741V → M in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036017
Natural varianti594 – 5941I → V.3 Publications
Corresponds to variant rs1866374 [ dbSNP | Ensembl ].
VAR_024530
Natural varianti869 – 8691E → G.
Corresponds to variant rs16876070 [ dbSNP | Ensembl ].
VAR_030347
Natural varianti1296 – 12961P → L.
Corresponds to variant rs34093016 [ dbSNP | Ensembl ].
VAR_034105
Natural varianti1917 – 19171S → R.
Corresponds to variant rs13153166 [ dbSNP | Ensembl ].
VAR_056123

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L06237 mRNA. Translation: AAA18904.1.
BN001084 mRNA. Translation: CAM06633.1.
AC012609 Genomic DNA. No translation available.
AC093218 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95697.1.
CCDSiCCDS4012.1.
RefSeqiNP_005900.2. NM_005909.3.
UniGeneiHs.335079.

Genome annotation databases

EnsembliENST00000296755; ENSP00000296755; ENSG00000131711.
GeneIDi4131.
KEGGihsa:4131.
UCSCiuc003kbw.4. human.

Polymorphism databases

DMDMi317373388.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L06237 mRNA. Translation: AAA18904.1 .
BN001084 mRNA. Translation: CAM06633.1 .
AC012609 Genomic DNA. No translation available.
AC093218 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95697.1 .
CCDSi CCDS4012.1.
RefSeqi NP_005900.2. NM_005909.3.
UniGenei Hs.335079.

3D structure databases

ProteinModelPortali P46821.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110304. 45 interactions.
DIPi DIP-33474N.
IntActi P46821. 28 interactions.
MINTi MINT-243072.
STRINGi 9606.ENSP00000296755.

PTM databases

PhosphoSitei P46821.

Polymorphism databases

DMDMi 317373388.

Proteomic databases

MaxQBi P46821.
PaxDbi P46821.
PRIDEi P46821.

Protocols and materials databases

DNASUi 4131.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296755 ; ENSP00000296755 ; ENSG00000131711 .
GeneIDi 4131.
KEGGi hsa:4131.
UCSCi uc003kbw.4. human.

Organism-specific databases

CTDi 4131.
GeneCardsi GC05P071438.
HGNCi HGNC:6836. MAP1B.
HPAi CAB009792.
HPA022275.
MIMi 157129. gene.
neXtProti NX_P46821.
PharmGKBi PA30581.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00550000074593.
HOGENOMi HOG000063256.
HOVERGENi HBG052409.
InParanoidi P46821.
KOi K10429.
OMAi RTPVQDH.
OrthoDBi EOG773XKP.
PhylomeDBi P46821.
TreeFami TF350229.

Miscellaneous databases

ChiTaRSi MAP1B. human.
GeneWikii MAP1B.
GenomeRNAii 4131.
NextBioi 16218.
PROi P46821.
SOURCEi Search...

Gene expression databases

Bgeei P46821.
CleanExi HS_MAP1B.
ExpressionAtlasi P46821. baseline and differential.
Genevestigatori P46821.

Family and domain databases

Gene3Di 3.60.15.10. 2 hits.
InterProi IPR001279. Beta-lactamas-like.
IPR026074. MAP1.
IPR027321. MAP1B.
IPR000102. MAP1B_neuraxin.
[Graphical view ]
PANTHERi PTHR13843. PTHR13843. 1 hit.
PTHR13843:SF5. PTHR13843:SF5. 1 hit.
Pfami PF00414. MAP1B_neuraxin. 5 hits.
[Graphical view ]
PROSITEi PS00230. MAP1B_NEURAXIN. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of human microtubule-associated protein 1B and the identification of a related gene on chromosome 15."
    Lien L.L., Feener C., Fischbach N., Kunkel L.M.
    Genomics 22:273-280(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-594.
    Tissue: Fetal brain.
  2. "Hmob3 brain-specific sequence is a part of phylogenetically conserved human MAP1B gene 3'-untranslated region."
    Dergunova L.V., Raevskaya N.M., Vladychenskaya I.P., Limborska S.A.
    Biomol. Eng. 20:91-96(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-594.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-594.
  5. Bienvenut W.V., Pchelintsev N., Adams P.D.
    Submitted (OCT-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-31; 55-64; 90-98; 391-429; 520-531; 1052-1070; 1233-1250; 1276-1287; 1462-1476; 1834-1958 AND 1898-1908, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Lung fibroblast.
  6. Lubec G., Afjehi-Sadat L., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2347-2370 AND 2382-2409, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  7. "Microtubule-associated protein 1B: a neuronal binding partner for gigaxonin."
    Ding J., Liu J.-J., Kowal A.S., Nardine T., Bhattacharya P., Lee A., Yang Y.
    J. Cell Biol. 158:427-433(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAN.
  8. "Cloning of a novel neuronally expressed orphan G-protein-coupled receptor which is up-regulated by erythropoietin, interacts with microtubule-associated protein 1b and colocalizes with the 5-hydroxytryptamine 2a receptor."
    Maurer M.H., Gruenewald S., Gassler N., Rossner M., Propst F., Wuerz R., Weber D., Kuner T., Kuschinsky W., Schneider A.
    J. Neurochem. 91:1007-1017(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMEM185A.
  9. "Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival."
    Allen E., Ding J., Wang W., Pramanik S., Chou J., Yau V., Yang Y.
    Nature 438:224-228(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAN.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-992; SER-995; SER-1016; SER-1265; SER-1276; SER-1280; THR-1282; SER-1396; SER-1400; SER-1427; SER-1438; SER-1443; SER-1618; SER-1620; SER-1625; SER-1779; SER-1782 AND THR-1788, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  13. "MAP1 structural organization in Drosophila: in vivo analysis of FUTSCH reveals heavy- and light-chain subunits generated by proteolytic processing at a conserved cleavage site."
    Zou B., Yan H., Kawasaki F., Ordway R.W.
    Biochem. J. 414:63-71(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE SITE.
  14. "DAPK-1 binding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing."
    Harrison B., Kraus M., Burch L., Stevens C., Craig A., Gordon-Weeks P., Hupp T.R.
    J. Biol. Chem. 283:9999-10014(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DAPK1.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1779, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831; SER-832; SER-1396; SER-1400 AND SER-1501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828; SER-831; SER-832; SER-937; SER-992; SER-995; SER-1016; SER-1144; SER-1154; SER-1156; SER-1208; SER-1252; SER-1256; SER-1260; SER-1265; THR-1282; SER-1378; SER-1387; SER-1389; SER-1400; SER-1427; SER-1438; SER-1443; SER-1501; SER-1653; SER-1779; SER-1782; SER-1785; THR-1788; SER-1797; SER-1915; SER-1917; SER-1965; SER-2271 AND SER-2289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites."
    Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B., Zhong Q.
    Nature 502:254-257(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP1LC3B.
  24. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-326 AND MET-574.

Entry informationi

Entry nameiMAP1B_HUMAN
AccessioniPrimary (citable) accession number: P46821
Secondary accession number(s): A2BDK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3